The structure of chromophore-grafted Amyloid-β 12-28 dimers in the gas-phase: FRET-experiments guided modelling - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Physical Chemistry Chemical Physics Année : 2016

The structure of chromophore-grafted Amyloid-β 12-28 dimers in the gas-phase: FRET-experiments guided modelling

Résumé

We present theoretical modelling, ion mobility spectrometry and action-FRET experiments for chromophore-grafted amyloid-β12–28 dimers. A first-principles global minimum search based on replica-exchange molecular dynamics (REMD) leads to a compact structure with strong interstrand interactions. We use REMD with a distance restraint that implements an adaptive effective bias upon average FRET-efficiencies and thus guides the sampling by the action-FRET measurement. This procedure leads to a pair of weakly interacting peptides. Ion-mobility confirms that the weakly interacting structure and not the global minimum with strongly interacting peptides is populated in the experiment. The presence of a high energy barrier between the two structural families, as evidenced from the MD data, suggests that a kinetically trapped structure is observed in the experiment.
Fichier principal
Vignette du fichier
The structure of chromophore-grafted Amyloid B dimers the gas phase.pdf (713.5 Ko) Télécharger le fichier
SuplementaryInformation_Proofstage_250216.pdf (582.56 Ko) Télécharger le fichier
Origine : Fichiers produits par l'(les) auteur(s)
Origine : Fichiers produits par l'(les) auteur(s)
Loading...

Dates et versions

hal-01344513 , version 1 (12-07-2016)

Identifiants

Citer

Alexander Kulesza, Steven Daly, Chang Min Choi, Anne-Laure Simon, Fabien Chirot, et al.. The structure of chromophore-grafted Amyloid-β 12-28 dimers in the gas-phase: FRET-experiments guided modelling. Physical Chemistry Chemical Physics, 2016, 18 (13), pp.9061-9069. ⟨10.1039/c6cp00263c⟩. ⟨hal-01344513⟩
131 Consultations
220 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More